5ZHQ

Crystal structure of Scylla paramamosain arginine kinase

Summary for 5ZHQ

• Entry DOI: 10.2210/pdb5zhq/pdb
• Descriptor: Arginine kinase, SULFATE ION (2 entities in total)
• Functional Keywords: food allergy, sea food allergy, arginine kinase, allergen
• Biological source: Scylla paramamosain (Mud crab)
• Total number of polymer chains: 2
• Total formula weight: 81370.14

Authors

Yang, Y.,Jin, T.C.,Liu, G.M. (deposition date: 2018-03-13, release date: 2019-03-20, Last modification date: 2025-09-17)

Primary citation

Yang, Y.,Liu, G.Y.,Yang, H.,Hu, M.J.,Cao, M.J.,Su, W.J.,Jin, T.,Liu, G.M.
Crystal structure determination of Scylla paramamosain arginine kinase, an allergen that may cause cross-reactivity among invertebrates.
Food Chem, 271:597-605, 2019

PubMed Abstract: Shellfish are one of the most common causes of food allergy. Arginine kinase (AK) is known as an important allergen in shellfish. In the present study, AK from crab (Scylla paramamosain) was purified and its crystal structure was determined. A comparison of AK from S. paramamosain to AKs of other species showed high amino acid sequence and secondary structure identity, while the superposition of crystal structures of AKs from different species revealed only slight differences. Similarity of the linear epitope regions among species was observed in the epitope alignment of AKs; conformational epitopes were located in the regions where secondary structure was conserved. The structure of S. paramamosain AK is an accurate template for the analysis of the IgE binding pattern, and the structure conservation and epitope similarity of AKs among species could help to inform our understanding of the cross-reactivity and contribute to the prediction of cross-reactivity related epitopes.

PubMed: 30236721
DOI: 10.1016/j.foodchem.2018.08.003

Experimental method

X-RAY DIFFRACTION (3.002 Å)